BMRB Entry 18642
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18642
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Title: Protein structure PubMed: 23770917
Deposition date: 2012-08-06 Original release date: 2013-06-10
Authors: Mercier, Pascal; Spratt, Donald; Manczyk, Noah; Shaw, Gary
Citation: Spratt, Donald; Julio Martinez-Torres, R.; Noh, Yeong; Mercier, Pascal; Manczyk, Noah; Barber, Kathryn; Aguirre, Jacob; Burchell, Lynn; Purkiss, Andrew; Walden, Helen; Shaw, Gary. "A molecular explanation for the recessive nature of parkin-linked Parkinson's disease." Nat. Commun. 4, 1983-1983 (2013).
Assembly members:
Protein, polymer, 68 residues, 7669.769 Da.
ZINC ION, non-polymer, 65.409 Da.
Natural source: Common Name: Fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Protein: GSAEARWDEASNVTIKVSTK
PCPKCRTPTERDGGCMHMVC
TRAGCGFEWCWVCQTEWTRD
CMGAHWFG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 256 |
| 15N chemical shifts | 63 |
| 1H chemical shifts | 388 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Protein | 1 |
| 2 | ZINC ION_1 | 2 |
| 3 | ZINC ION_2 | 2 |
Entities:
Entity 1, Protein 68 residues - 7669.769 Da.
N-terminal GS sequence results from the cleavage site
| 1 | GLY | SER | ALA | GLU | ALA | ARG | TRP | ASP | GLU | ALA | ||||
| 2 | SER | ASN | VAL | THR | ILE | LYS | VAL | SER | THR | LYS | ||||
| 3 | PRO | CYS | PRO | LYS | CYS | ARG | THR | PRO | THR | GLU | ||||
| 4 | ARG | ASP | GLY | GLY | CYS | MET | HIS | MET | VAL | CYS | ||||
| 5 | THR | ARG | ALA | GLY | CYS | GLY | PHE | GLU | TRP | CYS | ||||
| 6 | TRP | VAL | CYS | GLN | THR | GLU | TRP | THR | ARG | ASP | ||||
| 7 | CYS | MET | GLY | ALA | HIS | TRP | PHE | GLY |
Entity 2, ZINC ION_1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: TRIS 20 mM; sodium chloride 120 mM; DTT 5 mM; Protein, [U-98% 15N], 500 uM; H2O 90%; D2O 10%
sample_2: TRIS 20 mM; sodium chloride 120 mM; DTT 5 mM; Protein, [U-98% 13C; U-98% 15N], 500 uM; H2O 90%; D2O 10%
sample_3: TRIS 20 mM; sodium chloride 120 mM; DTT 5 mM; Protein, [U-98% 13C; U-98% 15N], 500 uM; D2O 100%
sample_conditions_1: ionic strength: 0.120 M; pH: 7.25; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)HD | sample_2 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCDCE)HE | sample_2 | isotropic | sample_conditions_1 |
Software:
VNMRJ vVarian VnmrJ 2.2D, Varian - collection
NMRPipe v2011.084.20.33, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw vVer 5.7 Rev 2011.084.20.33, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v8.2.33 with Java 1.6.0_31, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH v2.31, Schwieters, Kuszewski, Tjandra and Clore - refinement
TALOS vTALOSPlus, Cornilescu, Delaglio and Bax - geometry optimization
Procheck v3.5.4, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 18990 |
| PDB | |
| GB | AAL13983 AAM18800 AAM43930 AAN12154 AAN12155 |
| REF | NP_730600 NP_730601 XP_001956965 XP_001973584 XP_001984548 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts